Protocadherins: a large family of cadherin-related molecules in central nervous system.

Sano, Kenji; Tanihara, Hidenobu; Heimark, Ronald L.; Obata, Shuichi; Davidson, Mari K.; John, Tom St.; Taketani, Shigeru; Suzuki, Shintaro

doi:10.1002/j.1460-2075.1993.tb05878.x

Cited by 365 publications

(295 citation statements)

References 46 publications

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“…Interaction of the γ-Pcdh C-terminal constant domain with FAK and PYK2 was demonstrated to inhibit the activity of these tyrosine kinases (14), and the γ-Pcdhs also can inhibit canonical Wnt signaling in vitro (15). Cell adhesion mediated by trans interactions between clustered Pcdhs has been reported in several studies (7,(16)(17)(18)(19)(20)(21). With one exception (19), the sparse extant data are consistent with a cadherin-like homophilic mode of Pcdh interaction.…”

mentioning

confidence: 67%

“…Previous studies of interactions among clustered Pcdhs used a wide variety of methods, including aggregation of transfected L929 cells (16,17), K562 cells (20), or HEK293 cells (7); recruitment of Pcdhs to cell-cell contacts in HEK293 cells (18,21); and aggregation of beads coated with ectodomains (19). We tested several of these methods and found that only cell aggregation assays using the human leukemia line K562 were suitable for our experiments.…”

Section: γ-Pcdhs Mediate Trans Interactions With Properties Distinct mentioning

confidence: 99%

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Combinatorial homophilic interaction between γ-protocadherin multimers greatly expands the molecular diversity of cell adhesion

Schreiner

Weiner

2010

Proc. Natl. Acad. Sci. U.S.A.

234

436

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The specificity of interactions between neurons is believed to be mediated by diverse cell adhesion molecules, including members of the cadherin superfamily. Whereas mechanisms of classical cadherin adhesion have been studied extensively, much less is known about the related protocadherins (Pcdhs), which together make up the majority of the superfamily. Here we use quantitative cell aggregation assays and biochemical analyses to characterize cis and trans interactions among the 22-member γ-Pcdh family, which have been shown to be critical for the control of synaptogenesis and neuronal survival. We show that γ-Pcdh isoforms engage in trans interactions that are strictly homophilic. In contrast to classical cadherins, γ-Pcdh interactions are only partially Ca 2+ -dependent, and their specificity is mediated through the second and third extracellular cadherin (EC) domains (EC2 and EC3), rather than through EC1. The γ-Pcdhs also interact both covalently and noncovalently in the cis-orientation to form multimers both in vitro and in vivo. In contrast to γ-Pcdh trans interactions, cis interactions are highly promiscuous, with no isoform specificity. We present data supporting a model in which γ-Pcdh cistetramers represent the unit of their adhesive trans interactions. Unrestricted tetramerization in cis, coupled with strictly homophilic interactions in trans, predicts that the 22 γ-Pcdhs could form 234,256 distinct adhesive interfaces. Given the demonstrated role of the γ-Pcdhs in synaptogenesis, our data have important implications for the molecular control of neuronal specificity.cadherin | calcium-dependent | synaptogenesis | recognition | trafficking

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mentioning

confidence: 67%

Section: γ-Pcdhs Mediate Trans Interactions With Properties Distinct mentioning

confidence: 99%

Combinatorial homophilic interaction between γ-protocadherin multimers greatly expands the molecular diversity of cell adhesion

Schreiner

Weiner

2010

Proc. Natl. Acad. Sci. U.S.A.

234

436

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“…DISCUSSION In this report, we have described the isolation of a novel type II human cadherin molecule. Although many cadherins and cadherin-related molecules have been isolated by PCR (10,25), this is the first report of a cadherin molecule being isolated by virtue of its association with ␤-catenin. Cadherin-14 has several cytoplasmic amino acid sequences that differ from those used for PCR cloning.…”

Section: The Nucleotide Sequence(s) Reported In This Paper Has Been Smentioning

confidence: 95%

Identification of Human Cadherin-14, a Novel Neurally Specific Type II Cadherin, by Protein Interaction Cloning

Shibata¹,

Shimoyama²,

Gotoh³

et al. 1997

Journal of Biological Chemistry

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Cadherins, a family of Ca 2؉ -dependent cell-cell adhesion molecules, mediate neural cell-cell interactions and may play important roles in neural development. By searching for molecules that interact with ␤-catenin, a cytoplasmic regulator of cadherins, we have identified a new member of the cadherin family, which we named human cadherin-14. Cadherin-14 had high amino acid sequence homology with the type II subgroup of cadherins and was broadly expressed in the central nervous system. Cadherin-14 is a novel neurally specific cell-cell adhesion molecule and may regulate neural morphogenesis.

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“…Primers for protocadherin, pc-f2 (forward) and r2 (reverse), were virtually identical to those described previously (Sano et al, 1993). The sequences were 5Ј-CCG AAT TCA ARS SNN TNG AYT WYG A-3Ј and 5Ј-CCG GAT CCN NNG GNG CRT TRT CRT T-3Ј, respectively.…”

Section: Oligonucleotides For Cadherins and Protocadherinsmentioning

confidence: 99%

Zebrafish protocadherin 10 is involved in paraxial mesoderm development and somitogenesis

Murakami

Hijikata

Matsukawa

et al. 2005

Developmental Dynamics

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Here, we present the first report of the molecular cloning of zebrafish protocadherin 10 (Pcdh10, OLprotocadherin) and describe its functional analyses in the development of segmental plate. Epitope-tagged Pcdh10 expressed in embryos was localized on cell peripheries of adjacent cells. In situ hybridization showed that pcdh10 was expressed in the paraxial mesoderm (PAM) and developing somites, and in the pineal body, the diencephalon, and the vicinity of otocysts. Expression in PAM increased in the last few presumptive somites, reached the maximum level in the latest segmenting somites, and decreased thereafter during somite maturation. These expression patterns suggested that Pcdh10 is involved in development of PAM and somites. This was confirmed by morpholino knockdown and dominant-negative inhibition of Pcdh10 in embryos, which disturbed movements of PAM cells and somite segmentation. Comparative studies showed that pcdh10 expression lasted up to approximately three times longer in maturing somites than that of paraxial protocadherin (pcdh8). They also indicated that the adaxial cells expressed pcdh8 but not pcdh10. We propose that Pcdh10 is involved in the morphogenic movements of PAM cells and somite segmentation and that differential adhesion of Pcdh8 and Pcdh10 plays a role in the morphogenic machinery of somites and adaxial cells. Developmental Dynamics 235:506 -514, 2006.

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Protocadherins: a large family of cadherin-related molecules in central nervous system.

Cited by 365 publications

References 46 publications

Combinatorial homophilic interaction between γ-protocadherin multimers greatly expands the molecular diversity of cell adhesion

Combinatorial homophilic interaction between γ-protocadherin multimers greatly expands the molecular diversity of cell adhesion

Identification of Human Cadherin-14, a Novel Neurally Specific Type II Cadherin, by Protein Interaction Cloning

Zebrafish protocadherin 10 is involved in paraxial mesoderm development and somitogenesis

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